A commentary is offered on the spectroscopic way to characterize axial amine-iron ligation in a heme protein. This is of use to determine whether a lysine replaces the methionine ligand in the alkaline form of c-type cytochromes.
Characterization of Mutant Met100Lys of Cytochrome c-550 from Thiobacillus versutus with Lysine-Histidine Heme Ligation / Sola, Marco. - In: CHEMTRACTS. INORGANIC CHEMISTRY. - ISSN 1051-7227. - STAMPA. - 6:(1994), pp. 125-131.
Characterization of Mutant Met100Lys of Cytochrome c-550 from Thiobacillus versutus with Lysine-Histidine Heme Ligation.
SOLA, Marco
1994
Abstract
A commentary is offered on the spectroscopic way to characterize axial amine-iron ligation in a heme protein. This is of use to determine whether a lysine replaces the methionine ligand in the alkaline form of c-type cytochromes.
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